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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0011155,
umls-concept:C0017082,
umls-concept:C0020291,
umls-concept:C0030705,
umls-concept:C0033684,
umls-concept:C0042037,
umls-concept:C0061338,
umls-concept:C0219750,
umls-concept:C0392760,
umls-concept:C0475344,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C2003939
|
| pubmed:issue |
3
|
| pubmed:dateCreated |
1985-3-18
|
| pubmed:abstractText |
Urine specimens from two sibs affected with cerebroside sulfatase activator deficiency were examined to ascertain whether the deficiency of the supplementary activator protein required for the enzymatic hydrolysis of cerebroside sulfate was also evident in urine. Material from chromatographic fractionations was examined for the activator activity to avoid ambiguities resulting from protein inhibition. There were substantial deficits in all chromatographic fractions corresponding to activator-containing fractions of control urines. Since patient urines contained elevated amounts of lactosylceramide, digalactosylceramide, and globotriaosylceramide and since similarities between activators for cerebroside sulfate and GM1 ganglioside hydrolyses had been noted previously, the chromatographic fractions were also examined for activators in other glycosphingolipid hydrolase systems. There was coincidence of activators for the GM1 ganglioside/beta-galactosidase and the globotriaosylceramide/alpha-galactosidase A reactions with the cerebroside sulfatase activator in control urine fractions, and the patients' urines were deficient in activator activities for the three reactions. Identity of the three activators was suggested and antiserum to purified GM1 ganglioside activator was used to test this possibility. There were depressed levels of cross-reacting material in fractions of patient urines by Ouchterlony double diffusion and in unfractionated urine by enzyme-linked immunosorbent assay. Purified activators for the cerebroside sulfate and GM1 ganglioside systems showed lines of identity with no spurring on Ouchterlony double diffusion, identical mobility on immunoelectrophoresis, and similar stimulatory activities toward hydrolysis of the three glycosphingolipid species by their respective enzymes. Finally, the three activator activities were retained by anti-GM1-activator IgG coupled to Sepharose 4B. The results suggest strongly that the same protein entity serves as activator for the enzymatic hydrolysis of cerebroside sulfate, GM1 ganglioside, and globotriaosylceramide.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/G(M1) Ganglioside,
http://linkedlifedata.com/resource/pubmed/chemical/G(M2) Ganglioside,
http://linkedlifedata.com/resource/pubmed/chemical/Gangliosides,
http://linkedlifedata.com/resource/pubmed/chemical/Globosides,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosphingolipids,
http://linkedlifedata.com/resource/pubmed/chemical/Hexosaminidases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trihexosylceramides,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Galactosidase,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase,
http://linkedlifedata.com/resource/pubmed/chemical/beta-N-Acetylhexosaminidases,
http://linkedlifedata.com/resource/pubmed/chemical/globotriaosylceramide
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
10
|
| pubmed:volume |
260
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1867-71
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2981875-Animals,
pubmed-meshheading:2981875-Enzyme Activation,
pubmed-meshheading:2981875-G(M1) Ganglioside,
pubmed-meshheading:2981875-G(M2) Ganglioside,
pubmed-meshheading:2981875-Gangliosides,
pubmed-meshheading:2981875-Globosides,
pubmed-meshheading:2981875-Glycosphingolipids,
pubmed-meshheading:2981875-Hexosaminidases,
pubmed-meshheading:2981875-Humans,
pubmed-meshheading:2981875-Hydrolysis,
pubmed-meshheading:2981875-Immunodiffusion,
pubmed-meshheading:2981875-Immunosorbent Techniques,
pubmed-meshheading:2981875-Protein Deficiency,
pubmed-meshheading:2981875-Proteins,
pubmed-meshheading:2981875-Proteinuria,
pubmed-meshheading:2981875-Rats,
pubmed-meshheading:2981875-Trihexosylceramides,
pubmed-meshheading:2981875-alpha-Galactosidase,
pubmed-meshheading:2981875-beta-Galactosidase,
pubmed-meshheading:2981875-beta-N-Acetylhexosaminidases
|
| pubmed:year |
1985
|
| pubmed:articleTitle |
Activator protein required for the enzymatic hydrolysis of cerebroside sulfate. Deficiency in urine of patients affected with cerebroside sulfatase activator deficiency and identity with activators for the enzymatic hydrolysis of GM1 ganglioside and globotriaosylceramide.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|